Abstract:
:Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Deficiencies in this enzyme have been linked to autoimmune diseases and neurological disorders. The x-ray crystal structure of CDO from Mus musculus was solved to a nominal resolution of 1.75 Angstroms. The sequence is 91% identical to that of a human homolog. The structure reveals that CDO adopts the typical beta-barrel fold of the cupin superfamily. The NE2 atoms of His-86, -88, and -140 provide the metal binding site. The structure further revealed a covalent linkage between the side chains of Cys-93 and Tyr-157, the cysteine of which is conserved only in eukaryotic proteins. Metal analysis showed that the recombinant enzyme contained a mixture of iron, nickel, and zinc, with increased iron content associated with increased catalytic activity. Details of the predicted active site are used to present and discuss a plausible mechanism of action for the enzyme.
journal_name
Proc Natl Acad Sci U S Aauthors
McCoy JG,Bailey LJ,Bitto E,Bingman CA,Aceti DJ,Fox BG,Phillips GN Jrdoi
10.1073/pnas.0509262103keywords:
subject
Has Abstractpub_date
2006-02-28 00:00:00pages
3084-9issue
9eissn
0027-8424issn
1091-6490pii
0509262103journal_volume
103pub_type
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